Small-angle X-ray scattering and structural modeling of full-length: Cellobiohydrolase I from Trichoderma harzianum

Cellobiohydrolases hydrolyze cellulose releasing cellobiose units. They are very important for a number of biotechnological applications, such as, for example, production of cellulosic ethanol and cotton fiber processing. The Trichoderma cellobiohydrolase I (CBH1 or Cel7A) is an industrially important exocellulase. It exhibits a typical two domain architecture, with a small C-terminal cellulose-binding domain and a large N-terminal catalytic core domain, connected by an O-glycosylated linker peptide. The mechanism by which the linker mediates the concerted action of the two domains remains a conundrum. Here, we probe the protein shape and domain organization of the CBH1 of Trichoderma harzianum (ThCel7A) by small angle X-ray scattering (SAXS) and structural modeling. Our SAXS data shows that ThCel7A linker is partially-extended in solution. Structural modeling suggests that this linker conformation is stabilized by inter- and intra-molecular interactions involving the linker peptide and its O-glycosylations. © 2013 Springer Science+Business Media Dordrecht.

Sodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: Dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies

Glossoscolex paulistus (HbGp) hemoglobin is an oligomeric protein, presenting a quaternary structure constituted by 144 globin and 36 non-globin chains (named linkers) with a total molecular mass of 3.6MDa. SDS effects on the oxy-HbGp thermal stability were studied, by DLS and SAXS, at pH 5.0, 7.0 and 9.0. DLS and SAXS data show that the SDS-oxy-HbGp interactions induce a significant decrease of the protein thermal stability, with the formation of larger aggregates, at pH 5.0. At pH 7.0, oxy-HbGp undergoes complete oligomeric dissociation, with increase of temperature, in the presence of SDS. Besides, oxy-HbGp 3.0mg/mL, pH 7.0, in the presence of SDS, has the oligomeric dissociation process reduced as compared to 0.5mg/mL of protein. At pH 9.0, oxy-HbGp starts to dissociate at 20°C, and the protein is totally dissociated at 50°C. The thermal dissociation kinetic data show that oxy-HbGp oligomeric dissociation at pH 7.0, in the presence of SDS, is strongly dependent on the protein concentration. At 0.5mg/mL of protein, the oligomeric dissociation is complete and fast at 40 and 42°C, with kinetic constants of (2.1±0.2)×10-4 and (5.5±0.4)×10-4s-1, respectively, at 0.6mmol/L SDS. However, at 3.0mg/mL, the oligomeric dissociation process starts at 46°C, and only partial dissociation, accompanied by aggregates formation is observed. Moreover, our data show, for the first time, that, for 3.0mg/mL of protein, the oligomeric dissociation, denaturation and aggregation phenomena occur simultaneously, in the presence of SDS. Our present results on the surfactant-HbGp interactions and the protein thermal unfolding process correspond to a step forward in the understanding of SDS effects. © 2013 Elsevier B.V.

Some mathematical aspects and scattering amplitudes in the pure spinor formalism

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Study of double parton scattering using W+2-jet events in proton-proton collisions at root s=7 TeV

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Interpolating scattering amplitudes between the instant form and the front form of relativistic dynamics

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

N-point tree-level scattering amplitude in the new Berkovits' string

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Massless scattering at special kinematics as Jacobi polynomials

We study the scattering equations recently proposed by Cachazo, He and Yuan in the special kinematics where their solutions can be identified with the zeros of the Jacobi polynomials. This allows for a non-trivial two-parameter family of kinematics. We present explicit and compact formulas for the n-gluon and n-graviton partial scattering amplitudes for our special kinematics in terms of Jacobi polynomials. We also provide alternative expressions in terms of gamma functions. We give an interpretation of the common reduced determinant appearing in the amplitudes as the product of the squares of the eigenfrequencies of small oscillations of a system whose equilibrium is the solutions of the scattering equations.

Scattering Amplitudes Interpolating Between Instant Form and Front Form of Relativistic Dynamics

Among the three forms of relativistic Hamiltonian dynamics proposed by Dirac in 1949, the front form has the largest number of kinematic generators. This distinction provides useful consequences in the analysis of physical observables in hadron physics. Using the method of interpolation between the instant form and the front form, we introduce the interpolating scattering amplitude that links the corresponding time-ordered amplitudes between the two forms of dynamics and provide the physical meaning of the kinematic transformations as they allow the invariance of each individual time-ordered amplitude for an arbitrary interpolation angle. We discuss the rationale for using front form dynamics, nowadays known as light-front dynamics (LFD), and present a few explicit examples of hadron phenomenology that LFD uniquely can offer from first-principles quantum chromodynamics. In particular, model-independent constraints are provided for the analyses of deuteron form factors and the N Delta transition form factors at large momentum transfer squared Q(2). The swap of helicity amplitudes between the collinear and non-collinear kinematics is also discussed in deeply virtual Compton scattering.

Cetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: Dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Scattering and bound states of fermions in a mixed vector-scalar smooth step potential

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Detection of trace levels of atrazine using surface-enhanced Raman scattering and information visualization

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Release of Cyanopyridine from a Ruthenium Complex Adsorbed on Gold: Surface-Enhanced Raman Scattering, Electrochemistry, and Density Functional Theory Analyses

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Non-renormalization conditions for four-gluon scattering in supersymmetric string and field theory

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Causal approach for the electron-positron scattering in generalized quantum electrodynamics

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Encapsulation of paclitaxel into a bio-nanocomposite. a study combining inelastic neutron scattering to thermal analysis and infrared spectroscopy

The anticancer drug paclitaxel was encapsulated into a bio-nanocomposite formed by magnetic nanoparticles, chitosan and apatite. The aim of this drug carrier is to provide a new perspective against breast cancer. The dynamics of the pure and encapsulated drug were investigated in order to verify possible molecular changes caused by the encapsulation, as well as to follow which interactions may occur between paclitaxel and the composite. Fourier transformed infrared spectroscopy, thermal analysis, inelastic and quasi-elastic neutron scattering experiments were performed. These very preliminary results suggest the successful encapsulation of the drug.